Cathepsin L Protein (His Tag) (recombinant mouse)

Protein Construction: A DNA sequence encoding the mouse CTSL (P06797) (Met 1-Asn 334) was expressed, with a C-terminal polyhistidine tag. Sequence: Met 1-Asn 334. Fusion tag: C-His Endotoxin: < 1.0 EU per µg of the protein as determined by the LAL method. Protein function: Cathepsin L is a lysosomal cysteine protease that plays a major role in intracellular protein catabolism, and is potent in degrading collagen, laminin, elastin, as well as alpha-1 protease inhibitor and other structural proteins of basement membranes. It is secreted by liver flukes at all stages of their development in the mammalian host, are believed to play important roles in facilitating parasite migration (tissue degradation), feeding and immuno-evasion. Like many proteases, Cathepsin L is synthesized as an inactive preproenzyme, and cleavage of the 96-residue proregion is necessary to generate the fully active 221-residue mature enzyme. Studies have demonstrated that cleavage of the proregion occur autocatalytically under acidic conditions. The enzyme takes part in nutrient acquisition by catabolizing host proteins to absorbable peptides, facilitates the migration of the parasite through the host intestine and liver by cleaving interstitial matrix proteins such as fibronectin, laminin and native collage Protein function: Important for the overall degradation of proteins in lysosomes. [The UniProt Consortium]